ID IMP1L_HUMAN Reviewed; 166 AA.
AC Q96LU5; D3DQZ7; Q96SH9;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 24-JAN-2024, entry version 157.
DE RecName: Full=Mitochondrial inner membrane protease subunit 1;
DE EC=3.4.21.-;
DE AltName: Full=IMP1-like protein;
GN Name=IMMP1L;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15814844; DOI=10.1091/mbc.e04-12-1086;
RA Burri L., Strahm Y., Hawkins C.J., Gentle I.E., Puryer M.A., Verhagen A.,
RA Callus B., Vaux D., Lithgow T.;
RT "Mature DIABLO/Smac is produced by the IMP protease complex on the
RT mitochondrial inner membrane.";
RL Mol. Biol. Cell 16:2926-2933(2005).
CC -!- FUNCTION: Catalyzes the removal of transit peptides required for the
CC targeting of proteins from the mitochondrial matrix, across the inner
CC membrane, into the inter-membrane space. Known to process the nuclear
CC encoded protein DIABLO. {ECO:0000269|PubMed:15814844}.
CC -!- SUBUNIT: Heterodimer of 2 subunits, IMMPL1 and IMMPL2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:15814844}.
CC -!- SIMILARITY: Belongs to the peptidase S26 family. IMP1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC39221.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK057788; BAB71573.1; -; mRNA.
DR EMBL; AL133295; CAC39221.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471064; EAW68239.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68240.1; -; Genomic_DNA.
DR EMBL; BC023595; AAH23595.1; -; mRNA.
DR CCDS; CCDS7874.1; -.
DR RefSeq; NP_001291203.1; NM_001304274.1.
DR RefSeq; NP_659418.1; NM_144981.2.
DR RefSeq; XP_005252869.1; XM_005252812.3.
DR RefSeq; XP_011518244.1; XM_011519942.1.
DR RefSeq; XP_011518245.1; XM_011519943.2.
DR RefSeq; XP_011518246.1; XM_011519944.2.
DR RefSeq; XP_011518247.1; XM_011519945.2.
DR RefSeq; XP_011518248.1; XM_011519946.2.
DR RefSeq; XP_011518249.1; XM_011519947.2.
DR RefSeq; XP_016872794.1; XM_017017305.1.
DR AlphaFoldDB; Q96LU5; -.
DR SMR; Q96LU5; -.
DR BioGRID; 128195; 247.
DR ComplexPortal; CPX-6244; Mitochondrial inner membrane peptidase complex.
DR IntAct; Q96LU5; 238.
DR MINT; Q96LU5; -.
DR STRING; 9606.ENSP00000278200; -.
DR MEROPS; S26.002; -.
DR iPTMnet; Q96LU5; -.
DR PhosphoSitePlus; Q96LU5; -.
DR BioMuta; IMMP1L; -.
DR DMDM; 74752020; -.
DR EPD; Q96LU5; -.
DR jPOST; Q96LU5; -.
DR MassIVE; Q96LU5; -.
DR MaxQB; Q96LU5; -.
DR PaxDb; 9606-ENSP00000278200; -.
DR PeptideAtlas; Q96LU5; -.
DR ProteomicsDB; 77251; -.
DR Pumba; Q96LU5; -.
DR Antibodypedia; 49000; 90 antibodies from 25 providers.
DR DNASU; 196294; -.
DR Ensembl; ENST00000278200.5; ENSP00000278200.1; ENSG00000148950.11.
DR Ensembl; ENST00000532287.6; ENSP00000435576.1; ENSG00000148950.11.
DR GeneID; 196294; -.
DR KEGG; hsa:196294; -.
DR MANE-Select; ENST00000532287.6; ENSP00000435576.1; NM_001304274.2; NP_001291203.1.
DR UCSC; uc001msy.1; human.
DR AGR; HGNC:26317; -.
DR CTD; 196294; -.
DR DisGeNET; 196294; -.
DR GeneCards; IMMP1L; -.
DR HGNC; HGNC:26317; IMMP1L.
DR HPA; ENSG00000148950; Low tissue specificity.
DR MIM; 612323; gene.
DR neXtProt; NX_Q96LU5; -.
DR OpenTargets; ENSG00000148950; -.
DR PharmGKB; PA142671655; -.
DR VEuPathDB; HostDB:ENSG00000148950; -.
DR eggNOG; KOG0171; Eukaryota.
DR GeneTree; ENSGT00550000075025; -.
DR HOGENOM; CLU_028723_4_3_1; -.
DR InParanoid; Q96LU5; -.
DR OMA; CKGPSME; -.
DR OrthoDB; 447775at2759; -.
DR PhylomeDB; Q96LU5; -.
DR TreeFam; TF315083; -.
DR PathwayCommons; Q96LU5; -.
DR SignaLink; Q96LU5; -.
DR BioGRID-ORCS; 196294; 10 hits in 1116 CRISPR screens.
DR ChiTaRS; IMMP1L; human.
DR GenomeRNAi; 196294; -.
DR Pharos; Q96LU5; Tbio.
DR PRO; PR:Q96LU5; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q96LU5; Protein.
DR Bgee; ENSG00000148950; Expressed in endothelial cell and 185 other cell types or tissues.
DR ExpressionAtlas; Q96LU5; baseline and differential.
DR Genevisible; Q96LU5; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; NAS:ComplexPortal.
DR GO; GO:0042720; C:mitochondrial inner membrane peptidase complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; IBA:GO_Central.
DR GO; GO:0006465; P:signal peptide processing; NAS:ComplexPortal.
DR CDD; cd06530; S26_SPase_I; 1.
DR Gene3D; 2.10.109.10; Umud Fragment, subunit A; 1.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR InterPro; IPR019533; Peptidase_S26.
DR NCBIfam; TIGR02227; sigpep_I_bact; 1.
DR PANTHER; PTHR12383:SF33; MITOCHONDRIAL INNER MEMBRANE PROTEASE SUBUNIT 1; 1.
DR PANTHER; PTHR12383; PROTEASE FAMILY S26 MITOCHONDRIAL INNER MEMBRANE PROTEASE-RELATED; 1.
DR Pfam; PF10502; Peptidase_S26; 2.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Membrane; Mitochondrion; Mitochondrion inner membrane; Protease;
KW Reference proteome.
FT CHAIN 1..166
FT /note="Mitochondrial inner membrane protease subunit 1"
FT /id="PRO_0000259573"
FT ACT_SITE 40
FT /evidence="ECO:0000250"
FT ACT_SITE 83
FT /evidence="ECO:0000250"
SQ SEQUENCE 166 AA; 18504 MW; 53E4EB65757BA71A CRC64;
MLRGVLGKTF RLVGYTIQYG CIAHCAFEYV GGVVMCSGPS MEPTIQNSDI VFAENLSRHF
YGIQRGDIVI AKSPSDPKSN ICKRVIGLEG DKILTTSPSD FFKSHSYVPM GHVWLEGDNL
QNSTDSRCYG PIPYGLIRGR IFFKIWPLSD FGFLRASPNG HRFSDD
//
